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Q5VZK9 (LR16A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat-containing protein 16A
Alternative name(s):
CARMIL homolog
Gene names
Name:LRRC16A
Synonyms:CARMIL, CARMIL1a, LRRC16
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1371 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization By similarity. May control actin dynamics in lamellipodia. Required for cell migration. Ref.3 Ref.4

Subunit structure

Interacts via its C-terminus with CAPZA2 in cytoplasm; interaction is essential for lamellipodial protrusion and cell translocation By similarity. Homodimer. Ref.3

Subcellular location

Cell projectionlamellipodium. Cytoplasm. Note: Colocalized with F-actin in lamellipodia but not with F-actin in stress fibers. Also found on macropinosomes. Ref.3

Tissue specificity

Expressed in lung, placenta, small intestine, liver, thymus, colon, skeletal muscle, heart and brain. Higher expression in kidney. Ref.4

Sequence similarities

Belongs to the CARMIL family.

Contains 11 LRR (leucine-rich) repeats.

Sequence caution

The sequence BAA90912.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5VZK9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5VZK9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1177-1221: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5VZK9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     486-499: SLDISDNGLESDLS → QLGTRYRNAVLRVY
     500-1371: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q5VZK9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
     292-337: GVSSLSIQFA...SLSANPLTAS → ETTTKIKRQN...NYYSDFSHDG
     338-1371: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13711371Leucine-rich repeat-containing protein 16A
PRO_0000325815

Regions

Repeat245 – 26925LRR 1
Repeat275 – 29824LRR 2
Repeat304 – 32724LRR 3
Repeat336 – 36328LRR 4
Repeat391 – 41828LRR 5
Repeat423 – 44725LRR 6
Repeat481 – 50626LRR 7
Repeat543 – 56624LRR 8
Repeat570 – 59324LRR 9
Repeat654 – 67825LRR 10
Repeat958 – 98124LRR 11
Region958 – 1082125Inhibits capping activity of CAPZA2 By similarity
Coiled coil710 – 73425 Potential
Compositional bias1243 – 12508Poly-Ser

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue9161Phosphothreonine Ref.6
Modified residue9681Phosphoserine Ref.6 Ref.8 Ref.11
Modified residue10671Phosphoserine Ref.9
Modified residue12881Phosphoserine Ref.6 Ref.9 Ref.11
Modified residue12911Phosphoserine Ref.6
Modified residue13151Phosphoserine Ref.11
Modified residue13311Phosphoserine Ref.6 Ref.9 Ref.11
Modified residue13601Phosphoserine Ref.11
Cross-link593Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Natural variations

Alternative sequence1 – 161161Missing in isoform 4.
VSP_032415
Alternative sequence292 – 33746GVSSL…PLTAS → ETTTKIKRQNVPTVLQTYLV VCPSDYQPCPLPLGKDNYYS DFSHDG in isoform 4.
VSP_032416
Alternative sequence338 – 13711034Missing in isoform 4.
VSP_032417
Alternative sequence486 – 49914SLDIS…ESDLS → QLGTRYRNAVLRVY in isoform 3.
VSP_032418
Alternative sequence500 – 1371872Missing in isoform 3.
VSP_032419
Alternative sequence1177 – 122145Missing in isoform 2.
VSP_032420
Natural variant771V → I.
Corresponds to variant rs9358856 [ dbSNP | Ensembl ].
VAR_039923
Natural variant5451P → L.
Corresponds to variant rs12207840 [ dbSNP | Ensembl ].
VAR_039924
Natural variant6391A → G.
Corresponds to variant rs7454756 [ dbSNP | Ensembl ].
VAR_039925
Natural variant11171N → S.
Corresponds to variant rs9885914 [ dbSNP | Ensembl ].
VAR_039926

Experimental info

Sequence conflict2551N → D in BAC85701. Ref.1
Sequence conflict8891K → R in BAA90912. Ref.1
Sequence conflict12021G → S in ACI49709. Ref.1

Secondary structure

......... 1371
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 6DECD6387FD73DCE

FASTA1,371151,557
        10         20         30         40         50         60 
MTEESSDVPR ELIESIKDVI GRKIKISVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI 

        70         80         90        100        110        120 
PTKLELTFSY LEIHGVVCSK SAQMIVETEK CSISMKMASP EDVSEVLAHI GTCLRKIFPG 

       130        140        150        160        170        180 
LSPVRIMKKV SMEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACVCDWL GFSYREEVQW 

       190        200        210        220        230        240 
DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR 

       250        260        270        280        290        300 
VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSIQF 

       310        320        330        340        350        360 
AKLPKGLKHL NLSKTSLSPK GVNSLSQSLS ANPLTASTLV HLDLSGNVLR GDDLSHMYNF 

       370        380        390        400        410        420 
LAQPNAIVHL DLSNTECSLD MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF 

       430        440        450        460        470        480 
SSSLALMHIN LSGTKLSPEP LKALLLGLAC NHNLKGVSLD LSNCELRSGG AQVLEGCIAE 

       490        500        510        520        530        540 
IHNITSLDIS DNGLESDLST LIVWLSKNRS IQHLALGKNF NNMKSKNLTP VLDNLVQMIQ 

       550        560        570        580        590        600 
DEESPLQSLS LADSKLKTEV TIIINALGSN TSLTKVDISG NGMGDMGAKM LAKALQINTK 

       610        620        630        640        650        660 
LRTVIWDKNN ITAQGFQDIA VAMEKNYTLR FMPIPMYDAS QALKTNPEKT EDALQKIENY 

       670        680        690        700        710        720 
LLRNHETRKY LQEQAYRLQQ GIVTSTTQQM IDRICVKVQD HLNSLRNCGG DAIQEDLKSA 

       730        740        750        760        770        780 
ERLMRDAKNS KTLLPNLYHV GGASWAGASG LLSSPIQETL ESMAGEVTRV VDEQLKALLE 

       790        800        810        820        830        840 
SMVDAAENLC PNVMKKAHIR QDLIHASTEK ISIPRTFVKN VLLEQSGIDI LNKISEVKLT 

       850        860        870        880        890        900 
VASFLSDRIV DEILDALSHC HHKLADHFSR RGKTLPQQES LEIELAEEKP VKRSIITVEE 

       910        920        930        940        950        960 
LTEIERLEDL DTCMMTPKSK RKSIHSRMLR PVSRAFEMEF DLDKALEEVP IHIEDPPFPS 

       970        980        990       1000       1010       1020 
LRQEKRSSGF ISELPSEEGK KLEHFTKLRP KRNKKQQPTQ AAVCAANIVS QDGEQNGLMG 

      1030       1040       1050       1060       1070       1080 
RVDEGVDEFF TKKVTKMDSK KWSTRGSESH ELNEGGDEKK KRDSRKSSGF LNLIKSRSKS 

      1090       1100       1110       1120       1130       1140 
ERPPTILMTE EPSSPKGAVR SPPVDCPRKD TKAAEHNGNS ERIEEIKTPD SFEESQGEEI 

      1150       1160       1170       1180       1190       1200 
GKVERSDSKS SPQAGRRYGV QVMGSGLLAE MKAKQEKRAA CAQKKLGNDA VSQDSSSPAL 

      1210       1220       1230       1240       1250       1260 
SGVERSDGGG AVPKLHPGLP ENRFGLGTPE KNTKAEPKAE AGSRSRSSSS TPTSPKPLLQ 

      1270       1280       1290       1300       1310       1320 
SPKPSLAARP VIPQKPRTAS RPDDIPDSPS SPKVALLPPV LKKVPSDKER DGQSSPQPSP 

      1330       1340       1350       1360       1370 
RTFSQEVSRR SWGQQAQEYQ EQKQRSSSKD GHQGSKSNDS GEEAEKEFIF V 

« Hide

Isoform 2 [UniParc].

Checksum: BC4881025483CA27
Show »

FASTA1,326147,088
Isoform 3 [UniParc].

Checksum: A77D54FABEE374C8
Show »

FASTA49955,117
Isoform 4 [UniParc].

Checksum: 806D8D31AAC2A04A
Show »

FASTA17620,181

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-1371 (ISOFORM 2).
Tissue: Colon, Esophageal carcinoma and Teratocarcinoma.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Distinct roles for CARMIL isoforms in cell migration."
Liang Y., Niederstrasser H., Edwards M., Jackson C.E., Cooper J.A.
Mol. Biol. Cell 20:5290-5305(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[4]"Mammalian CARMIL inhibits actin filament capping by capping protein."
Yang C., Pring M., Wear M.A., Huang M., Cooper J.A., Svitkina T.M., Zigmond S.H.
Dev. Cell 9:209-221(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-593.
Tissue: Mammary cancer.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916; SER-968; SER-1288; SER-1291 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067; SER-1288 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1288; SER-1315; SER-1331 AND SER-1360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ009082 mRNA. Translation: ACI49709.1.
AK123817 mRNA. Translation: BAC85701.1.
AK125696 mRNA. Translation: BAC86250.1.
AK000055 mRNA. Translation: BAA90912.1. Different initiation.
AL160037, AL022170, AL024509 Genomic DNA. Translation: CAH72024.1.
AL022170, AL024509, AL160037 Genomic DNA. Translation: CAI21583.1.
AL024509, AL022170, AL160037 Genomic DNA. Translation: CAI21665.1.
RefSeqNP_060110.4. NM_017640.5.
UniGeneHs.649550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LK2X-ray2.20T961-1012[»]
3LK3X-ray2.68T964-1078[»]
ProteinModelPortalQ5VZK9.
SMRQ5VZK9. Positions 9-664, 961-1035.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120745. 6 interactions.
DIPDIP-56920N.
IntActQ5VZK9. 1 interaction.
MINTMINT-5005073.
STRING9606.ENSP00000331983.

PTM databases

PhosphoSiteQ5VZK9.

Polymorphism databases

DMDM74762279.

Proteomic databases

PaxDbQ5VZK9.
PeptideAtlasQ5VZK9.
PRIDEQ5VZK9.

Protocols and materials databases

DNASU55604.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329474; ENSP00000331983; ENSG00000079691. [Q5VZK9-1]
ENST00000377969; ENSP00000367206; ENSG00000079691. [Q5VZK9-4]
GeneID55604.
KEGGhsa:55604.
UCSCuc011djw.2. human. [Q5VZK9-1]

Organism-specific databases

CTD55604.
GeneCardsGC06P025279.
H-InvDBHIX0005632.
HGNCHGNC:21581. LRRC16A.
HPAHPA029038.
HPA029039.
MIM609593. gene.
neXtProtNX_Q5VZK9.
PharmGKBPA162394368.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239526.
HOGENOMHOG000230565.
HOVERGENHBG108094.
InParanoidQ5VZK9.
OMATLIVWLS.
OrthoDBEOG72JWFD.
PhylomeDBQ5VZK9.
TreeFamTF316381.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeQ5VZK9.
CleanExHS_LRRC16A.
GenevestigatorQ5VZK9.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSLRRC16A. human.
EvolutionaryTraceQ5VZK9.
GeneWikiLRRC16A.
GenomeRNAi55604.
NextBio35481565.
PROQ5VZK9.
SOURCESearch...

Entry information

Entry nameLR16A_HUMAN
AccessionPrimary (citable) accession number: Q5VZK9
Secondary accession number(s): B8X1J0 expand/collapse secondary AC list , Q6ZUH5, Q6ZW07, Q9NXU7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM